ID ALBU_HUMAN Reviewed; 609 AA. AC P02768; E7ESS9; O95574; P04277; Q13140; Q645G4; Q68DN5; Q6UXK4; Q86YG0; AC Q8IUK7; Q9P157; Q9P1I7; Q9UHS3; Q9UJZ0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 27-MAR-2024, entry version 288. DE RecName: Full=Albumin; DE Flags: Precursor; GN Name=ALB; GN ORFNames=GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, GN UNQ696/PRO1341; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-420. RX PubMed=6171778; DOI=10.1093/nar/9.22.6103; RA Lawn R.M., Adelman J., Bock S.C., Franke A.E., Houck C.M., Najarian R.C., RA Seeburg P.H., Wion K.L.; RT "The sequence of human serum albumin cDNA and its expression in E. coli."; RL Nucleic Acids Res. 9:6103-6114(1981). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-121. RX PubMed=6275391; DOI=10.1073/pnas.79.1.71; RA Dugaiczyk A., Law S.W., Dennison O.E.; RT "Nucleotide sequence and the encoded amino acids of human serum albumin RT mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 79:71-75(1982). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3009475; DOI=10.1016/s0021-9258(19)62680-3; RA Minghetti P.P., Ruffner D.E., Kuang W.J., Dennison O.E., Hawkins J.W., RA Beattie W.G., Dugaiczyk A.; RT "Molecular structure of the human albumin gene is revealed by nucleotide RT sequence within q11-22 of chromosome 4."; RL J. Biol. Chem. 261:6747-6757(1986). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Yang S., Zhang R.A., Qi Z.W., Yuan Z.Y.; RT "Human serum albumin."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIROSHIMA-1 LYS-378. RA Huang M.C., Wu H.T.; RT "The cDNA sequences of human serum albumin."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Hinchliffe E.; RT "Induction of galactose regulated gene expression in yeast."; RL Patent number EP0248637, 09-DEC-1987. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Yu Z., Fu Y.; RT "High expression HSA in Pichia for Pharmaceutical Use."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Wang F., Huang L.; RT "Cloning and sequence analysis of human albumin gene."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RA Kim J.W.; RT "Identification of a human cell growth inhibition gene."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal liver; RX PubMed=11483580; DOI=10.1101/gr.175501; RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.; RT "Gene expression profiling in human fetal liver and identification of RT tissue- and developmental-stage-specific genes through compiled expression RT profiles and efficient cloning of full-length cDNAs."; RL Genome Res. 11:1392-1403(2001). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-27. RC TISSUE=Liver; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Liver, and Skeletal muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-455. RC TISSUE=Liver; RA Menaya J., Parrilla R., Ayuso M.S.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. RX PubMed=2419329; DOI=10.1016/s0021-9258(17)35775-7; RA Urano Y., Watanabe K., Sakai M., Tamaoki T.; RT "The human albumin gene. Characterization of the 5' and 3' flanking regions RT and the polymorphic gene transcripts."; RL J. Biol. Chem. 261:3244-3251(1986). RN [19] RP PROTEIN SEQUENCE OF 25-609. RX PubMed=1225573; DOI=10.1016/0014-5793(75)80242-0; RA Meloun B., Moravek L., Kostka V.; RT "Complete amino acid sequence of human serum albumin."; RL FEBS Lett. 58:134-137(1975). RN [20] RP PROTEIN SEQUENCE OF 25-609. RA Brown J.R., Shockley P., Behrens P.Q.; RL (In) Bing D.H. (eds.); RL The chemistry and physiology of the human plasma proteins, pp.23-40, RL Pergamon Press, New York (1979). RN [21] RP PROTEIN SEQUENCE OF 25-44 AND 480-499. RC TISSUE=Heart; RX PubMed=7895732; DOI=10.1002/elps.11501501209; RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; RT "The human myocardial two-dimensional gel protein database: update 1994."; RL Electrophoresis 15:1459-1465(1994). RN [22] RP PROTEIN SEQUENCE OF 25-34. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [23] RP PROTEIN SEQUENCE OF 45-75; 98-130; 162-183; 239-254; 265-281; 287-298; RP 348-372; 397-434; 438-452; 500-543; 550-558; 570-581 AND 599-609, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [24] RP PROTEIN SEQUENCE OF 166-174. RX PubMed=3087352; DOI=10.1016/0006-291x(86)90429-8; RA Mogard M.H., Kobayashi R., Chen C.F., Lee T.D., Reeve J.R. Jr., RA Shively J.E., Walsh J.H.; RT "The amino acid sequence of kinetensin, a novel peptide isolated from RT pepsin-treated human plasma: homology with human serum albumin, neurotensin RT and angiotensin."; RL Biochem. Biophys. Res. Commun. 136:983-988(1986). RN [25] RP PROTEIN SEQUENCE OF 166-174. RX PubMed=2437111; DOI=10.1016/s0021-9258(18)45523-8; RA Carraway R.E., Mitra S.P., Cochrane D.E.; RT "Structure of a biologically active neurotensin-related peptide obtained RT from pepsin-treated albumin(s)."; RL J. Biol. Chem. 262:5968-5973(1987). RN [26] RP PROTEIN SEQUENCE OF 222-229, AND ASPIRIN-ACETYLATION AT LYS-223. RX PubMed=955075; DOI=10.1016/0014-5793(76)80496-6; RA Walker J.E.; RT "Lysine residue 199 of human serum albumin is modified by acetylsalicylic RT acid."; RL FEBS Lett. 66:173-175(1976). RN [27] RP PROTEIN SEQUENCE OF 250-264, GLYCATION AT LYS-75; LYS-161; LYS-186; RP LYS-249; LYS-257; LYS-300; LYS-337; LYS-347; LYS-375; LYS-402; LYS-437; RP LYS-468; LYS-560; LYS-549; LYS-569 AND LYS-597, LACK OF GLYCATION AT RP LYS-28; LYS-44; LYS-65; LYS-88; LYS-97; LYS-117; LYS-130; LYS-160; LYS-183; RP LYS-198; LYS-205; LYS-214; LYS-219; LYS-229; LYS-236; LYS-264; LYS-286; RP LYS-298; LYS-310; LYS-383; LYS-396; LYS-413; LYS-426; LYS-438; LYS-456; RP LYS-460; LYS-490; LYS-499; LYS-524; LYS-543; LYS-548; LYS-562; LYS-565; RP LYS-581; LYS-584; LYS-588 AND LYS-598, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15047055; DOI=10.1016/j.jasms.2003.11.014; RA Lapolla A., Fedele D., Reitano R., Arico N.C., Seraglia R., Traldi P., RA Marotta E., Tonani R.; RT "Enzymatic digestion and mass spectrometry in the study of advanced RT glycation end products/peptides."; RL J. Am. Soc. Mass Spectrom. 15:496-509(2004). RN [28] RP DISULFIDE BONDS. RA Saber M.A., Stockbauer P., Moravek L., Meloun B.; RT "Disulfide bonds in human serum albumin."; RL Collect. Czech. Chem. Commun. 42:564-579(1977). RN [29] RP BILIRUBIN-BINDING SITE. RX PubMed=656055; DOI=10.1042/bj1710453; RA Jacobsen C.; RT "Lysine residue 240 of human serum albumin is involved in high-affinity RT binding of bilirubin."; RL Biochem. J. 171:453-459(1978). RN [30] RP GLYCATION AT LYS-223 AND LYS-549. RX PubMed=6853480; DOI=10.1016/s0021-9258(18)32384-6; RA Garlick R.L., Mazer J.S.; RT "The principal site of nonenzymatic glycosylation of human serum albumin in RT vivo."; RL J. Biol. Chem. 258:6142-6146(1983). RN [31] RP FUNCTION. RX PubMed=6234017; DOI=10.1021/bi00305a003; RA Konopka K., Neilands J.B.; RT "Effect of serum albumin on siderophore-mediated utilization of transferrin RT iron."; RL Biochemistry 23:2122-2127(1984). RN [32] RP GLYCATION AT LYS-549. RX PubMed=6706980; DOI=10.1016/s0021-9258(17)43168-1; RA Shaklai N., Garlick R.L., Bunn H.F.; RT "Nonenzymatic glycosylation of human serum albumin alters its conformation RT and function."; RL J. Biol. Chem. 259:3812-3817(1984). RN [33] RP GLYCATION AT LYS-36; LYS-223; LYS-257; LYS-305; LYS-341; LYS-375; LYS-463; RP LYS-549 AND LYS-558. RX PubMed=3759977; DOI=10.1016/s0021-9258(18)67052-8; RA Iberg N., Fluckiger R.; RT "Nonenzymatic glycosylation of albumin in vivo. Identification of multiple RT glycosylated sites."; RL J. Biol. Chem. 261:13542-13545(1986). RN [34] RP INVOLVEMENT IN ANALBA. RX PubMed=8134387; DOI=10.1073/pnas.91.6.2275; RA Watkins S., Madison J., Galliano M., Minchiotti L., Putnam F.W.; RT "A nucleotide insertion and frameshift cause analbuminemia in an Italian RT family."; RL Proc. Natl. Acad. Sci. U.S.A. 91:2275-2279(1994). RN [35] RP INTERACTION WITH ALPHA-1-MICROGLOBULIN. RX PubMed=9183005; DOI=10.1111/j.1432-1033.1997.00676.x; RA Berggaard T., Thelin N., Falkenberg C., Enghild J.J., Akerstroem B.; RT "Prothrombin, albumin and immunoglobulin A form covalent complexes with RT alpha1-microglobulin in human plasma."; RL Eur. J. Biochem. 245:676-683(1997). RN [36] RP FUNCTION. RX PubMed=19021548; DOI=10.1042/bst0361317; RA Lu J., Stewart A.J., Sadler P.J., Pinheiro T.J., Blindauer C.A.; RT "Albumin as a zinc carrier: properties of its high-affinity zinc-binding RT site."; RL Biochem. Soc. Trans. 36:1317-1321(2008). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; THR-444 AND THR-446, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [39] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [40] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89 AND SER-513, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [41] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-558, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [42] RP PHOSPHORYLATION AT SER-29; SER-82; SER-89 AND THR-107. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [43] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [44] RP INTERACTION WITH FCGRT. RX PubMed=28330995; DOI=10.1073/pnas.1618291114; RA Pyzik M., Rath T., Kuo T.T., Win S., Baker K., Hubbard J.J., Grenha R., RA Gandhi A., Kraemer T.D., Mezo A.R., Taylor Z.S., McDonnell K., Nienaber V., RA Andersen J.T., Mizoguchi A., Blumberg L., Purohit S., Jones S.D., RA Christianson G., Lencer W.I., Sandlie I., Kaplowitz N., Roopenian D.C., RA Blumberg R.S.; RT "Hepatic FcRn regulates albumin homeostasis and susceptibility to liver RT injury."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E2862-E2871(2017). RN [45] RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS). RX PubMed=2727704; DOI=10.1126/science.2727704; RA Carter D.C., He X.-M., Munson S.H., Twigg P.D., Gernert K.M., Broom M.B., RA Miller T.Y.; RT "Three-dimensional structure of human serum albumin."; RL Science 244:1195-1198(1989). RN [46] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS). RX PubMed=2374930; DOI=10.1126/science.2374930; RA Carter D.C., He X.-M.; RT "Structure of human serum albumin."; RL Science 249:302-303(1990). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND FUNCTION. RX PubMed=1630489; DOI=10.1038/358209a0; RA He X.-M., Carter D.C.; RT "Atomic structure and chemistry of human serum albumin."; RL Nature 358:209-215(1992). RN [48] RP ERRATUM OF PUBMED:1630489. RA He X.-M., Carter D.C.; RL Nature 364:362-362(1993). RN [49] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=9731778; DOI=10.1038/1869; RA Curry S., Mandelkow H., Brick P., Franks N.; RT "Crystal structure of human serum albumin complexed with fatty acid reveals RT an asymmetric distribution of binding sites."; RL Nat. Struct. Biol. 5:827-835(1998). RN [50] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=10388840; DOI=10.1093/protein/12.6.439; RA Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K.; RT "Crystal structure of human serum albumin at 2.5-A resolution."; RL Protein Eng. 12:439-446(1999). RN [51] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-609. RX PubMed=10940303; DOI=10.1074/jbc.m005460200; RA Bhattacharya A.A., Curry S., Franks N.P.; RT "Binding of the general anesthetics propofol and halothane to human serum RT albumin. High resolution crystal structures."; RL J. Biol. Chem. 275:38731-38738(2000). RN [52] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=11743713; DOI=10.1006/jmbi.2000.5208; RA Petitpas I., Grune T., Bhattacharya A.A., Curry S.; RT "Crystal structures of human serum albumin complexed with monounsaturated RT and polyunsaturated fatty acids."; RL J. Mol. Biol. 314:955-960(2001). RN [53] {ECO:0007744|PDB:5IJF} RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-609 IN COMPLEX WITH ZINC, RP DISULFIDE BOND, AND MUTAGENESIS OF HIS-91. RX PubMed=28567254; DOI=10.1039/c6sc02267g; RA Handing K.B., Shabalin I.G., Kassaar O., Khazaipoul S., Blindauer C.A., RA Stewart A.J., Chruszcz M., Minor W.; RT "Circulatory zinc transport is controlled by distinct interdomain sites on RT mammalian albumins."; RL Chem. Sci. 7:6635-6648(2016). RN [54] RP VARIANT CANTERBURY ASN-337. RX PubMed=3828358; DOI=10.1016/0167-4838(87)90088-4; RA Brennan S.O., Herbert P.; RT "Albumin Canterbury (313 Lys-->Asn). A point mutation in the second domain RT of serum albumin."; RL Biochim. Biophys. Acta 912:191-197(1987). RN [55] RP VARIANT NASKAPI/MERSIN GLU-396, AND VARIANT MEXICO GLY-574. RX PubMed=3474609; DOI=10.1073/pnas.84.13.4413; RA Takahashi N., Takahashi Y., Blumberg B.S., Putnam F.W.; RT "Amino acid substitutions in genetic variants of human serum albumin and in RT sequences inferred from molecular cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4413-4417(1987). RN [56] RP VARIANT NAGASAKI-3 GLN-27, VARIANT YANOMAMA-2 GLU-396, VARIANT NAGASAKI-2 RP ASN-399, AND VARIANT MAKU GLU-565. RX PubMed=3479777; DOI=10.1073/pnas.84.22.8001; RA Takshashi N., Takahashi Y., Isobe T., Putnam F.W., Fujita M., Satoh C., RA Neel J.V.; RT "Amino acid substitutions in inherited albumin variants from Amerindian and RT Japanese populations."; RL Proc. Natl. Acad. Sci. U.S.A. 84:8001-8005(1987). RN [57] RP VARIANT FUKUOKA-2 HIS-23, VARIANT CHRISTCHURCH/HONOLULU-2 GLN-24, VARIANT RP TAGLIACOZZO ASN-337, AND VARIANT ALBUMIN B/OSAKA-2/PHNOM PHEN LYS-594. RX PubMed=2911589; DOI=10.1073/pnas.86.2.434; RA Arai K., Ishioka N., Huss K., Madison J., Putnam F.W.; RT "Identical structural changes in inherited albumin variants from different RT populations."; RL Proc. Natl. Acad. Sci. U.S.A. 86:434-438(1989). RN [58] RP VARIANT HONOLULU-2 GLN-24, VARIANT NAGASAKI-1 GLY-293, VARIANT HIROSHIMA-1 RP LYS-378, VARIANT TOCHIGI LYS-400, VARIANT HIROSHIMA-2 LYS-406, AND VARIANT RP OSAKA-2 LYS-594. RX PubMed=2762316; DOI=10.1073/pnas.86.16.6092; RA Arai K., Madison J., Huss K., Ishioka N., Satoh C., Fujita M., Neel J.V., RA Sakurabayashi I., Putnam F.W.; RT "Point substitutions in Japanese alloalbumins."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6092-6096(1989). RN [59] RP VARIANT HONOLULU-1 PRO-24, VARIANT HONOLULU-2 GLN-24, VARIANT NAGOYA RP LYS-143, VARIANT NEW GUINEA ASN-337, VARIANT MANAUS-1/LAMBADI LYS-525, RP VARIANT FUKUOKA-1 ASN-587, VARIANT OSAKA-1 LYS-589, AND VARIANT OSAKA-2 RP LYS-594. RX PubMed=2404284; DOI=10.1073/pnas.87.1.497; RA Arai K., Madison J., Shimuzu A., Putnam F.W.; RT "Point substitutions in albumin genetic variants from Asia."; RL Proc. Natl. Acad. Sci. U.S.A. 87:497-501(1990). RN [60] RP CHARACTERIZATION OF VARIANT REDHILL. RX PubMed=2104980; DOI=10.1073/pnas.87.1.26; RA Brennan S.O., Myles T., Peach R.J., Donaldson D., George P.M.; RT "Albumin Redhill (-1 Arg, 320 Ala-->Thr): a glycoprotein variant of human RT serum albumin whose precursor has an aberrant signal peptidase cleavage RT site."; RL Proc. Natl. Acad. Sci. U.S.A. 87:26-30(1990). RN [61] RP VARIANT VARESE HIS-23, VARIANT TORINO LYS-84, AND VARIANT VIBO VALENTIA RP LYS-106. RX PubMed=2247440; DOI=10.1073/pnas.87.22.8721; RA Galliano M., Minchiotti L., Porta F., Rossi A., Ferri G., Madison J., RA Watkins S., Putnam F.W.; RT "Mutations in genetic variants of human serum albumin found in Italy."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8721-8725(1990). RN [62] RP CHARACTERIZATION OF VARIANT VENEZIA. RX PubMed=2068071; DOI=10.1073/pnas.88.14.5959; RA Watkins S., Madison J., Davis E., Sakamoto Y., Galliano M., Minchiotti L., RA Putnam F.W.; RT "A donor splice mutation and a single-base deletion produce two carboxyl- RT terminal variants of human serum albumin."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5959-5963(1991). RN [63] RP VARIANT KOMAGOME-3 HIS-23, VARIANT IOWA CITY-2 VAL-25, VARIANT KOMAGOME-2 RP ARG-152, VARIANT IOWA CITY-1 VAL-389, AND VARIANT KOMAGOME-1 GLU-396. RX PubMed=1946412; DOI=10.1073/pnas.88.21.9853; RA Madison J., Arai K., Feld R.D., Kyle R.A., Watkins S., Davis E., RA Matsuda Y., Amaki I., Putnam F.W.; RT "Genetic variants of serum albumin in Americans and Japanese."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9853-9857(1991). RN [64] RP VARIANT CASEBROOK ASN-518. RX PubMed=1859851; DOI=10.1016/0925-4439(91)90023-3; RA Peach R.J., Brennan S.O.; RT "Structural characterization of a glycoprotein variant of human serum RT albumin: albumin Casebrook (494 Asp-->Asn)."; RL Biochim. Biophys. Acta 1097:49-54(1991). RN [65] RP VARIANT SONDRIO LYS-357, AND VARIANT PARIS-2 ASN-587. RX PubMed=1347703; DOI=10.1016/0167-4838(92)90207-t; RA Minchiotti L., Galliano M., Stoppini M., Ferri G., Crespeau H., Rochu D., RA Porta F.; RT "Two alloalbumins with identical electrophoretic mobility are produced by RT differently charged amino acid substitutions."; RL Biochim. Biophys. Acta 1119:232-238(1992). RN [66] RP VARIANT MALMO-I CYS-23, VARIANT MALMO-95 ASN-87, VARIANT MALMO-10 ARG-292, RP VARIANT MALMO-47 LYS-342, VARIANT MALMO-5 GLN-400, AND VARIANT MALMO-61 RP ALA-574. RX PubMed=1518850; DOI=10.1073/pnas.89.17.8225; RA Carlson J., Sakamoto Y., Laurell C.-B., Madison J., Watkins S., RA Putnam F.W.; RT "Alloalbuminemia in Sweden: structural study and phenotypic distribution of RT nine albumin variants."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8225-8229(1992). RN [67] RP VARIANT HERBORN GLU-264. RX PubMed=8513793; DOI=10.1111/j.1432-1033.1993.tb17939.x; RA Minchiotti L., Galliano M., Zapponi M.C., Tenni R.; RT "The structural characterization and bilirubin-binding properties of RT albumin Herborn, a [Lys240-->Glu] albumin mutant."; RL Eur. J. Biochem. 214:437-444(1993). RN [68] RP VARIANT HAWKES BAY PHE-201. RX PubMed=8347685; DOI=10.1016/0925-4439(93)90151-p; RA Brennan S.O., Fellowes A.P.; RT "Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl RT group at position 177."; RL Biochim. Biophys. Acta 1182:46-50(1993). RN [69] RP VARIANT ORTONOVO LYS-529. RX PubMed=7902134; DOI=10.1016/0925-4439(93)90117-j; RA Galliano M., Minchiotti L., Iadarola P., Stoppini M., Giagnoni P., RA Watkins S., Madison J., Putnam F.W.; RT "Protein and DNA sequence analysis of a 'private' genetic variant: albumin RT Ortonovo (Glu-505-->Lys)."; RL Biochim. Biophys. Acta 1225:27-32(1993). RN [70] RP VARIANT LARINO TYR-27, VARIANT TRADATE-2 GLN-249, AND VARIANT CASERTA RP ASN-300. RX PubMed=8022807; DOI=10.1073/pnas.91.14.6476; RA Madison J., Galliano M., Watkins S., Minchiotti L., Porta F., Rossi A., RA Putnam F.W.; RT "Genetic variants of human serum albumin in Italy: point mutants and a RT carboxyl-terminal variant."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6476-6480(1994). RN [71] RP VARIANT FDAH HIS-242. RX PubMed=8048949; DOI=10.1006/bbrc.1994.1998; RA Sunthornthepvarakul T., Angkeow P., Weiss R.E., Hayashi Y., Retetoff S.; RT "An identical missense mutation in the albumin gene results in familial RT dysalbuminemic hyperthyroxinemia in 8 unrelated families."; RL Biochem. Biophys. Res. Commun. 202:781-787(1994). RN [72] RP VARIANT FDAH HIS-242, AND PROTEIN SEQUENCE OF 25-51. RX PubMed=7852505; DOI=10.1210/jcem.80.2.7852505; RA Rushbrook J.I., Becker E., Schussler G.C., Divino C.M.; RT "Identification of a human serum albumin species associated with familial RT dysalbuminemic hyperthyroxinemia."; RL J. Clin. Endocrinol. Metab. 80:461-467(1995). RN [73] RP VARIANT FDAH PRO-242. RX PubMed=9329347; DOI=10.1210/jcem.82.10.4276; RA Wada N., Chiba H., Shimizu C., Kijima H., Kubo M., Koike T.; RT "A novel missense mutation in codon 218 of the albumin gene in a distinct RT phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese RT kindred."; RL J. Clin. Endocrinol. Metab. 82:3246-3250(1997). RN [74] RP VARIANT FDAH PRO-90. RX PubMed=9589637; DOI=10.1210/jcem.83.5.4815; RA Sunthornthepvarakul T., Likitmaskul S., Ngowngarmratana S., Angsusingha K., RA Kitvitayasak S., Scherberg N.H., Refetoff S.; RT "Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly RT inherited albumin defect."; RL J. Clin. Endocrinol. Metab. 83:1448-1454(1998). RN [75] RP VARIANT TYR-73, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Urine; RX PubMed=11680902; RX DOI=10.1002/1615-9861(200101)1:1<93::aid-prot93>3.0.co;2-3; RA Spahr C.S., Davis M.T., McGinley M.D., Robinson J.H., Bures E.J., RA Beierle J., Mort J., Courchesne P.L., Chen K., Wahl R.C., Yu W., Luethy R., RA Patterson S.D.; RT "Towards defining the urinary proteome using liquid chromatography-tandem RT mass spectrometry I. Profiling an unfractionated tryptic digest."; RL Proteomics 1:93-107(2001). RN [76] RP CHARACTERIZATION OF VARIANT KENITRA. RX PubMed=11168369; DOI=10.1046/j.1432-1033.2001.01899.x; RA Minchiotti L., Campagnoli M., Rossi A., Cosulich M.E., Monti M., Pucci P., RA Kragh-Hansen U., Granel B., Disdier P., Weiller P.J., Galliano M.; RT "A nucleotide insertion and frameshift cause albumin Kenitra, an extended RT and O-glycosylated mutant of human serum albumin with two additional RT disulfide bridges."; RL Eur. J. Biochem. 268:344-352(2001). CC -!- FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, CC bilirubin and drugs (Probable). Its main function is the regulation of CC the colloidal osmotic pressure of blood (Probable). Major zinc CC transporter in plasma, typically binds about 80% of all plasma zinc CC (PubMed:19021548). Major calcium and magnesium transporter in plasma, CC binds approximately 45% of circulating calcium and magnesium in plasma CC (By similarity). Potentially has more than two calcium-binding sites CC and might additionally bind calcium in a non-specific manner (By CC similarity). The shared binding site between zinc and calcium at CC residue Asp-273 suggests a crosstalk between zinc and calcium transport CC in the blood (By similarity). The rank order of affinity is zinc > CC calcium > magnesium (By similarity). Binds to the bacterial siderophore CC enterobactin and inhibits enterobactin-mediated iron uptake of E.coli CC from ferric transferrin, and may thereby limit the utilization of iron CC and growth of enteric bacteria such as E.coli (PubMed:6234017). Does CC not prevent iron uptake by the bacterial siderophore aerobactin CC (PubMed:6234017). {ECO:0000250|UniProtKB:P02769, CC ECO:0000269|PubMed:19021548, ECO:0000269|PubMed:6234017, CC ECO:0000305|PubMed:1630489}. CC -!- SUBUNIT: Interacts with FCGRT; this interaction regulates ALB CC homeostasis (PubMed:28330995). Interacts with TASOR (By similarity). In CC plasma, occurs in a covalently-linked complex with chromophore-bound CC alpha-1-microglobulin with molar ratio 1:2 and 1:1; this interaction CC does not prevent fatty acid binding to ALB. CC {ECO:0000250|UniProtKB:P07724, ECO:0000269|PubMed:28330995, CC ECO:0000269|PubMed:9183005}. CC -!- INTERACTION: CC P02768; P02768: ALB; NbExp=8; IntAct=EBI-714423, EBI-714423; CC P02768; P02786: TFRC; NbExp=2; IntAct=EBI-714423, EBI-355727; CC P02768-3; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-25830928, EBI-743960; CC P02768-3; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-25830928, EBI-25830200; CC P02768-3; Q07869: PPARA; NbExp=3; IntAct=EBI-25830928, EBI-78615; CC P02768-3; Q09028: RBBP4; NbExp=3; IntAct=EBI-25830928, EBI-620823; CC P02768-3; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-25830928, EBI-11525489; CC P02768-3; O76024: WFS1; NbExp=3; IntAct=EBI-25830928, EBI-720609; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P02768-1; Sequence=Displayed; CC Name=2; CC IsoId=P02768-2; Sequence=VSP_021275; CC Name=3; CC IsoId=P02768-3; Sequence=VSP_057389; CC -!- TISSUE SPECIFICITY: Plasma. CC -!- PTM: Kenitra variant is partially O-glycosylated at Thr-620. It has two CC new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606. CC -!- PTM: Glycated in diabetic patients. CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium. CC {ECO:0000269|PubMed:26091039}. CC -!- PTM: Acetylated on Lys-223 by acetylsalicylic acid. CC -!- POLYMORPHISM: A variant structure of albumin could lead to increased CC binding of zinc resulting in an asymptomatic augmentation of zinc CC concentration in the blood. The sequence shown is that of variant CC albumin A. CC -!- DISEASE: Hyperthyroxinemia, familial dysalbuminemic (FDAH) CC [MIM:615999]: A disorder characterized by abnormally elevated levels of CC total serum thyroxine (T4) in euthyroid patients. It is due to abnormal CC serum albumin that binds T4 with enhanced affinity. CC {ECO:0000269|PubMed:7852505, ECO:0000269|PubMed:8048949, CC ECO:0000269|PubMed:9329347, ECO:0000269|PubMed:9589637}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Analbuminemia (ANALBA) [MIM:616000]: A rare autosomal CC recessive disorder manifested by the presence of a very low amount of CC circulating serum albumin. Affected individuals manifest mild edema, CC hypotension, fatigue, and, occasionally, lower body lipodystrophy CC (mainly in adult females). The most common biochemical finding is CC hyperlipidemia, with a significant increase in the total and LDL CC cholesterol concentrations, but normal concentrations of HDL CC cholesterol and triglycerides. {ECO:0000269|PubMed:8134387}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE- CC ProRule:PRU00769}. CC -!- CAUTION: A peptide arising from positions 166 to 174 was originally CC (PubMed:3087352, PubMed:2437111) termed neurotensin-related peptide CC (NRP) or kinetensin and was thought to regulate fat digestion, lipid CC absorption, and blood flow. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF22034.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF69644.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAG35503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Albumin Website; CC URL="https://albumin.org"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Serum albumin entry; CC URL="https://en.wikipedia.org/wiki/Serum_albumin"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/alb/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V00494; CAA23753.1; -; mRNA. DR EMBL; V00495; CAA23754.1; -; mRNA. DR EMBL; M12523; AAA98797.1; -; Genomic_DNA. DR EMBL; M12523; AAA98798.1; -; Genomic_DNA. DR EMBL; AF190168; AAF01333.1; -; mRNA. DR EMBL; AF542069; AAN17825.1; -; mRNA. DR EMBL; A06977; CAA00606.1; -; mRNA. DR EMBL; AY728024; AAU21642.1; -; mRNA. DR EMBL; DQ986150; ABJ16448.1; -; mRNA. DR EMBL; AY544124; AAT11155.1; -; mRNA. DR EMBL; AY550967; AAT52213.1; -; mRNA. DR EMBL; AF116645; AAF71067.1; -; mRNA. DR EMBL; AF118090; AAF22034.1; ALT_INIT; mRNA. DR EMBL; AF119840; AAF69594.1; -; mRNA. DR EMBL; AF119890; AAF69644.1; ALT_INIT; mRNA. DR EMBL; AF130077; AAG35503.1; ALT_INIT; mRNA. DR EMBL; CR749331; CAH18185.1; -; mRNA. DR EMBL; EF649953; ABS29264.1; -; Genomic_DNA. DR EMBL; AC108157; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX05676.1; -; Genomic_DNA. DR EMBL; BC014308; AAH14308.1; -; mRNA. DR EMBL; BC034023; AAH34023.1; -; mRNA. DR EMBL; BC035969; AAH35969.1; -; mRNA. DR EMBL; BC036003; AAH36003.1; -; mRNA. DR EMBL; BC041789; AAH41789.1; -; mRNA. DR EMBL; U22961; AAA64922.1; -; mRNA. DR EMBL; AY358313; AAQ89947.1; -; mRNA. DR EMBL; AH002596; AAA51688.1; -; Genomic_DNA. DR CCDS; CCDS3555.1; -. [P02768-1] DR PIR; A93743; ABHUS. DR RefSeq; NP_000468.1; NM_000477.6. [P02768-1] DR PDB; 1AO6; X-ray; 2.50 A; A/B=25-609. DR PDB; 1BJ5; X-ray; 2.50 A; A=25-609. DR PDB; 1BKE; X-ray; 3.15 A; A=28-608. DR PDB; 1BM0; X-ray; 2.50 A; A/B=25-609. DR PDB; 1E78; X-ray; 2.60 A; A/B=25-609. DR PDB; 1E7A; X-ray; 2.20 A; A/B=25-609. DR PDB; 1E7B; X-ray; 2.38 A; A/B=25-609. DR PDB; 1E7C; X-ray; 2.40 A; A=25-609. DR PDB; 1E7E; X-ray; 2.50 A; A=25-609. DR PDB; 1E7F; X-ray; 2.43 A; A=25-609. DR PDB; 1E7G; X-ray; 2.50 A; A=25-609. DR PDB; 1E7H; X-ray; 2.43 A; A=25-609. DR PDB; 1E7I; X-ray; 2.70 A; A=25-609. DR PDB; 1GNI; X-ray; 2.40 A; A=25-609. DR PDB; 1GNJ; X-ray; 2.60 A; A=25-609. DR PDB; 1H9Z; X-ray; 2.50 A; A=25-609. DR PDB; 1HA2; X-ray; 2.50 A; A=25-609. DR PDB; 1HK1; X-ray; 2.65 A; A=25-609. DR PDB; 1HK2; X-ray; 2.80 A; A=25-609. DR PDB; 1HK3; X-ray; 2.80 A; A=25-609. DR PDB; 1HK4; X-ray; 2.40 A; A=25-609. DR PDB; 1HK5; X-ray; 2.70 A; A=25-609. DR PDB; 1N5U; X-ray; 1.90 A; A=25-609. DR PDB; 1O9X; X-ray; 3.20 A; A=25-609. DR PDB; 1TF0; X-ray; 2.70 A; A=25-596. DR PDB; 1UOR; X-ray; 2.80 A; A=25-609. DR PDB; 1YSX; NMR; -; A=409-609. DR PDB; 2BX8; X-ray; 2.70 A; A/B=25-609. DR PDB; 2BXA; X-ray; 2.35 A; A/B=25-609. DR PDB; 2BXB; X-ray; 3.20 A; A/B=25-609. DR PDB; 2BXC; X-ray; 3.10 A; A/B=25-609. DR PDB; 2BXD; X-ray; 3.05 A; A/B=25-609. DR PDB; 2BXE; X-ray; 2.95 A; A/B=25-609. DR PDB; 2BXF; X-ray; 2.95 A; A/B=25-609. DR PDB; 2BXG; X-ray; 2.70 A; A/B=25-609. DR PDB; 2BXH; X-ray; 2.25 A; A/B=25-609. DR PDB; 2BXI; X-ray; 2.50 A; A=25-609. DR PDB; 2BXK; X-ray; 2.40 A; A=25-609. DR PDB; 2BXL; X-ray; 2.60 A; A=25-609. DR PDB; 2BXM; X-ray; 2.50 A; A=25-609. DR PDB; 2BXN; X-ray; 2.65 A; A=25-609. DR PDB; 2BXO; X-ray; 2.60 A; A=25-609. DR PDB; 2BXP; X-ray; 2.30 A; A=25-609. DR PDB; 2BXQ; X-ray; 2.60 A; A=25-609. DR PDB; 2ESG; X-ray; -; C=25-609. DR PDB; 2I2Z; X-ray; 2.70 A; A=25-609. DR PDB; 2I30; X-ray; 2.90 A; A=25-609. DR PDB; 2N0X; NMR; -; A=432-447. DR PDB; 2VDB; X-ray; 2.52 A; A=30-608. DR PDB; 2VUE; X-ray; 2.42 A; A/B=25-609. DR PDB; 2VUF; X-ray; 3.05 A; A/B=25-609. DR PDB; 2XSI; X-ray; 2.70 A; A=25-609. DR PDB; 2XVQ; X-ray; 2.90 A; A/B=25-609. DR PDB; 2XVU; X-ray; 2.60 A; A/B=25-609. DR PDB; 2XVV; X-ray; 2.40 A; A=25-609. DR PDB; 2XVW; X-ray; 2.65 A; A=25-609. DR PDB; 2XW0; X-ray; 2.40 A; A/B=25-609. DR PDB; 2XW1; X-ray; 2.50 A; A/B=25-609. DR PDB; 2YDF; X-ray; 2.75 A; A/B=25-609. DR PDB; 3A73; X-ray; 2.19 A; A/B=25-609. DR PDB; 3B9L; X-ray; 2.60 A; A=25-609. DR PDB; 3B9M; X-ray; 2.70 A; A=25-609. DR PDB; 3CX9; X-ray; 2.80 A; A=27-608. DR PDB; 3JQZ; X-ray; 3.30 A; A/B=25-609. DR PDB; 3JRY; X-ray; 2.30 A; A/B=25-609. DR PDB; 3LU6; X-ray; 2.70 A; A/B=25-609. DR PDB; 3LU7; X-ray; 2.80 A; A/B=25-609. DR PDB; 3LU8; X-ray; 2.60 A; A/B=25-609. DR PDB; 3SQJ; X-ray; 2.05 A; A/B=27-608. DR PDB; 3TDL; X-ray; 2.60 A; A=25-609. DR PDB; 3UIV; X-ray; 2.20 A; A/H=25-609. DR PDB; 4BKE; X-ray; 2.35 A; A=1-609. DR PDB; 4E99; X-ray; 2.30 A; A=25-609. DR PDB; 4EMX; X-ray; 2.30 A; A/B=25-609. DR PDB; 4G03; X-ray; 2.22 A; A/B=25-609. DR PDB; 4G04; X-ray; 2.30 A; A/B=25-609. DR PDB; 4HGK; X-ray; 3.04 A; A/B=25-609. DR PDB; 4HGM; X-ray; 2.34 A; B=25-609. DR PDB; 4IW1; X-ray; 2.56 A; A=25-609. DR PDB; 4IW2; X-ray; 2.41 A; A=25-609. DR PDB; 4K2C; X-ray; 3.23 A; A/B=25-609. DR PDB; 4K71; X-ray; 2.40 A; A/D=25-609. DR PDB; 4L8U; X-ray; 2.01 A; A=25-609. DR PDB; 4L9K; X-ray; 2.40 A; A/B=25-609. DR PDB; 4L9Q; X-ray; 2.70 A; A/B=25-609. DR PDB; 4LA0; X-ray; 2.40 A; A/B=25-609. DR PDB; 4LB2; X-ray; 2.80 A; A/B=25-609. DR PDB; 4LB9; X-ray; 2.70 A; A=25-609. DR PDB; 4N0F; X-ray; 3.02 A; D/G/J/M=25-609. DR PDB; 4N0U; X-ray; 3.80 A; D=27-609. DR PDB; 4S1Y; X-ray; 3.16 A; A=25-609. DR PDB; 4Z69; X-ray; 2.19 A; A/I=25-609. DR PDB; 5FUO; X-ray; 3.60 A; A=25-609. DR PDB; 5GIX; X-ray; 2.80 A; A/B=27-607. DR PDB; 5GIY; X-ray; 2.54 A; A=27-607. DR PDB; 5ID7; X-ray; 2.26 A; A/B=25-609. DR PDB; 5IFO; X-ray; 3.20 A; A=25-609. DR PDB; 5IJF; X-ray; 2.65 A; A=25-609. DR PDB; 5UJB; X-ray; 2.70 A; A/B=1-609. DR PDB; 5VNW; X-ray; 2.60 A; A/B=25-609. DR PDB; 5X52; X-ray; 3.00 A; A/B=25-609. DR PDB; 5YB1; X-ray; 2.62 A; A/B=27-607. DR PDB; 5YOQ; X-ray; 2.65 A; A/B=25-609. DR PDB; 5Z0B; X-ray; 2.17 A; A/B/C=25-609. DR PDB; 6A7P; X-ray; 2.28 A; A/B=25-609. DR PDB; 6EZQ; X-ray; 2.39 A; A=25-609. DR PDB; 6HSC; X-ray; 1.90 A; A/B=1-609. DR PDB; 6JE7; X-ray; 3.90 A; A=26-608. DR PDB; 6L4K; X-ray; 2.09 A; A/I=27-607. DR PDB; 6M4R; X-ray; 2.49 A; A/B=25-609. DR PDB; 6M58; X-ray; 2.95 A; A/B=25-609. DR PDB; 6M5D; X-ray; 2.60 A; A=28-606. DR PDB; 6M5E; X-ray; 2.80 A; A/B/C=25-609. DR PDB; 6QIO; X-ray; 1.95 A; A=25-609. DR PDB; 6QIP; X-ray; 2.45 A; A=25-609. DR PDB; 6R7S; X-ray; 2.21 A; A=25-609. DR PDB; 6WUW; X-ray; 2.20 A; A/B=25-609. DR PDB; 6XV0; X-ray; 3.00 A; A=25-609. DR PDB; 6YG9; X-ray; 1.89 A; A=25-609. DR PDB; 6ZL1; X-ray; 3.27 A; A/B=1-609. DR PDB; 7A9C; X-ray; 2.75 A; AAA=25-609. DR PDB; 7AAE; X-ray; 2.27 A; AAA=26-609. DR PDB; 7AAI; X-ray; 2.10 A; AAA=26-609. DR PDB; 7D6J; X-ray; 3.29 A; A/B=25-609. DR PDB; 7DJN; X-ray; 2.04 A; A/B=25-609. DR PDB; 7DL4; X-ray; 2.40 A; A=25-609. DR PDB; 7EEK; X-ray; 2.50 A; A/B=26-608. DR PDB; 7FFR; X-ray; 2.31 A; A=25-609. DR PDB; 7FFS; X-ray; 2.05 A; A=25-609. DR PDB; 7JWN; X-ray; 2.60 A; A=26-609. DR PDB; 7OV1; X-ray; 1.90 A; A/B=1-609. DR PDB; 7OV5; X-ray; 1.90 A; A/B=1-609. DR PDB; 7OV6; X-ray; 1.90 A; A/B=1-609. DR PDB; 7QFE; X-ray; 2.20 A; A=25-609. DR PDB; 7VR0; X-ray; 1.98 A; A=25-609. DR PDB; 7VR9; X-ray; 2.30 A; A/B=25-609. DR PDB; 7WKZ; X-ray; 2.99 A; A/B=25-609. DR PDB; 7WLF; X-ray; 2.40 A; A=25-609. DR PDB; 7WOJ; X-ray; 2.89 A; A=1-609. DR PDB; 7WOK; X-ray; 2.90 A; A/B=1-609. DR PDB; 7WZ9; X-ray; 2.83 A; A=27-607. DR PDB; 7X7X; X-ray; 2.10 A; A/B=25-609. DR PDB; 7Y2D; X-ray; 2.00 A; A=27-607. DR PDB; 7Z57; X-ray; 2.20 A; A=26-609. DR PDB; 8A9Q; X-ray; 2.00 A; A/B=25-609. DR PDB; 8CKS; X-ray; 2.60 A; A=25-609. DR PDB; 8EW4; X-ray; 2.40 A; A=25-609. DR PDB; 8EW7; X-ray; 3.30 A; A=25-609. DR PDB; 8EY5; X-ray; 3.10 A; A=25-609. DR PDB; 8H0O; X-ray; 2.48 A; A=25-609. DR PDB; 8Q3F; EM; 3.77 A; A=25-609. DR PDBsum; 1AO6; -. DR PDBsum; 1BJ5; -. DR PDBsum; 1BKE; -. DR PDBsum; 1BM0; -. DR PDBsum; 1E78; -. DR PDBsum; 1E7A; -. DR PDBsum; 1E7B; -. DR PDBsum; 1E7C; -. DR PDBsum; 1E7E; -. DR PDBsum; 1E7F; -. DR PDBsum; 1E7G; -. DR PDBsum; 1E7H; -. DR PDBsum; 1E7I; -. DR PDBsum; 1GNI; -. DR PDBsum; 1GNJ; -. DR PDBsum; 1H9Z; -. DR PDBsum; 1HA2; -. DR PDBsum; 1HK1; -. DR PDBsum; 1HK2; -. DR PDBsum; 1HK3; -. DR PDBsum; 1HK4; -. DR PDBsum; 1HK5; -. DR PDBsum; 1N5U; -. DR PDBsum; 1O9X; -. DR PDBsum; 1TF0; -. DR PDBsum; 1UOR; -. DR PDBsum; 1YSX; -. DR PDBsum; 2BX8; -. DR PDBsum; 2BXA; -. DR PDBsum; 2BXB; -. DR PDBsum; 2BXC; -. DR PDBsum; 2BXD; -. DR PDBsum; 2BXE; -. DR PDBsum; 2BXF; -. DR PDBsum; 2BXG; -. DR PDBsum; 2BXH; -. DR PDBsum; 2BXI; -. DR PDBsum; 2BXK; -. DR PDBsum; 2BXL; -. DR PDBsum; 2BXM; -. DR PDBsum; 2BXN; -. DR PDBsum; 2BXO; -. DR PDBsum; 2BXP; -. DR PDBsum; 2BXQ; -. DR PDBsum; 2ESG; -. DR PDBsum; 2I2Z; -. DR PDBsum; 2I30; -. DR PDBsum; 2N0X; -. DR PDBsum; 2VDB; -. DR PDBsum; 2VUE; -. DR PDBsum; 2VUF; -. DR PDBsum; 2XSI; -. DR PDBsum; 2XVQ; -. DR PDBsum; 2XVU; -. DR PDBsum; 2XVV; -. DR PDBsum; 2XVW; -. DR PDBsum; 2XW0; -. DR PDBsum; 2XW1; -. DR PDBsum; 2YDF; -. DR PDBsum; 3A73; -. DR PDBsum; 3B9L; -. DR PDBsum; 3B9M; -. DR PDBsum; 3CX9; -. DR PDBsum; 3JQZ; -. DR PDBsum; 3JRY; -. DR PDBsum; 3LU6; -. DR PDBsum; 3LU7; -. DR PDBsum; 3LU8; -. DR PDBsum; 3SQJ; -. DR PDBsum; 3TDL; -. DR PDBsum; 3UIV; -. DR PDBsum; 4BKE; -. DR PDBsum; 4E99; -. DR PDBsum; 4EMX; -. DR PDBsum; 4G03; -. DR PDBsum; 4G04; -. DR PDBsum; 4HGK; -. DR PDBsum; 4HGM; -. DR PDBsum; 4IW1; -. DR PDBsum; 4IW2; -. DR PDBsum; 4K2C; -. DR PDBsum; 4K71; -. DR PDBsum; 4L8U; -. DR PDBsum; 4L9K; -. DR PDBsum; 4L9Q; -. DR PDBsum; 4LA0; -. DR PDBsum; 4LB2; -. DR PDBsum; 4LB9; -. DR PDBsum; 4N0F; -. DR PDBsum; 4N0U; -. DR PDBsum; 4S1Y; -. DR PDBsum; 4Z69; -. DR PDBsum; 5FUO; -. DR PDBsum; 5GIX; -. DR PDBsum; 5GIY; -. DR PDBsum; 5ID7; -. DR PDBsum; 5IFO; -. DR PDBsum; 5IJF; -. DR PDBsum; 5UJB; -. DR PDBsum; 5VNW; -. DR PDBsum; 5X52; -. DR PDBsum; 5YB1; -. DR PDBsum; 5YOQ; -. DR PDBsum; 5Z0B; -. DR PDBsum; 6A7P; -. DR PDBsum; 6EZQ; -. DR PDBsum; 6HSC; -. DR PDBsum; 6JE7; -. DR PDBsum; 6L4K; -. DR PDBsum; 6M4R; -. DR PDBsum; 6M58; -. DR PDBsum; 6M5D; -. DR PDBsum; 6M5E; -. DR PDBsum; 6QIO; -. DR PDBsum; 6QIP; -. DR PDBsum; 6R7S; -. DR PDBsum; 6WUW; -. DR PDBsum; 6XV0; -. DR PDBsum; 6YG9; -. DR PDBsum; 6ZL1; -. DR PDBsum; 7A9C; -. DR PDBsum; 7AAE; -. DR PDBsum; 7AAI; -. DR PDBsum; 7D6J; -. DR PDBsum; 7DJN; -. DR PDBsum; 7DL4; -. DR PDBsum; 7EEK; -. DR PDBsum; 7FFR; -. DR PDBsum; 7FFS; -. DR PDBsum; 7JWN; -. DR PDBsum; 7OV1; -. DR PDBsum; 7OV5; -. DR PDBsum; 7OV6; -. DR PDBsum; 7QFE; -. DR PDBsum; 7VR0; -. DR PDBsum; 7VR9; -. DR PDBsum; 7WKZ; -. DR PDBsum; 7WLF; -. DR PDBsum; 7WOJ; -. DR PDBsum; 7WOK; -. DR PDBsum; 7WZ9; -. DR PDBsum; 7X7X; -. DR PDBsum; 7Y2D; -. DR PDBsum; 7Z57; -. DR PDBsum; 8A9Q; -. DR PDBsum; 8CKS; -. DR PDBsum; 8EW4; -. DR PDBsum; 8EW7; -. DR PDBsum; 8EY5; -. DR PDBsum; 8H0O; -. DR PDBsum; 8Q3F; -. DR AlphaFoldDB; P02768; -. DR BMRB; P02768; -. DR EMDB; EMD-18126; -. DR PCDDB; P02768; -. DR SASBDB; P02768; -. DR SMR; P02768; -. DR BioGRID; 106715; 383. DR DIP; DIP-29902N; -. DR IntAct; P02768; 216. DR MINT; P02768; -. DR STRING; 9606.ENSP00000295897; -. DR BindingDB; P02768; -. DR ChEMBL; CHEMBL3253; -. DR DrugBank; DB08496; (R)-warfarin. DR DrugBank; DB07517; 3-CARBOXY-4-METHYL-5-PROPYL-2-FURANPROPIONIC. DR DrugBank; DB12001; Abemaciclib. DR DrugBank; DB05812; Abiraterone. DR DrugBank; DB14973; Abrocitinib. DR DrugBank; DB11703; Acalabrutinib. DR DrugBank; DB01418; Acenocoumarol. DR DrugBank; DB01614; Acepromazine. DR DrugBank; DB00316; Acetaminophen. DR DrugBank; DB00414; Acetohexamide. DR DrugBank; DB09347; Acetrizoic acid. DR DrugBank; DB06151; Acetylcysteine. DR DrugBank; DB00459; Acitretin. DR DrugBank; DB00787; Acyclovir. DR DrugBank; DB00640; Adenosine. DR DrugBank; DB00802; Alfentanil. DR DrugBank; DB00346; Alfuzosin. DR DrugBank; DB00404; Alprazolam. DR DrugBank; DB01370; Aluminium. DR DrugBank; DB14517; Aluminium phosphate. DR DrugBank; DB14518; Aluminum acetate. DR DrugBank; DB01118; Amiodarone. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB01060; Amoxicillin. DR DrugBank; DB00415; Ampicillin. DR DrugBank; DB00276; Amsacrine. DR DrugBank; DB06728; Aniline. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB04557; Arachidonic Acid. DR DrugBank; DB09229; Aranidipine. DR DrugBank; DB11217; Arbutin. DR DrugBank; DB00278; Argatroban. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB14185; Aripiprazole lauroxil. DR DrugBank; DB09204; Arotinolol. DR DrugBank; DB01169; Arsenic trioxide. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB09274; Artesunate. DR DrugBank; DB00126; Ascorbic acid. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB01072; Atazanavir. DR DrugBank; DB00335; Atenolol. DR DrugBank; DB00289; Atomoxetine. DR DrugBank; DB01076; Atorvastatin. DR DrugBank; DB00995; Auranofin. DR DrugBank; DB06237; Avanafil. DR DrugBank; DB07402; Azapropazone. DR DrugBank; DB00993; Azathioprine. DR DrugBank; DB08822; Azilsartan medoxomil. DR DrugBank; DB16703; Belumosudil. DR DrugBank; DB00245; Benzatropine. DR DrugBank; DB01086; Benzocaine. DR DrugBank; DB01053; Benzylpenicillin. DR DrugBank; DB00443; Betamethasone. DR DrugBank; DB14669; Betamethasone phosphate. DR DrugBank; DB13909; Bismuth subgallate. DR DrugBank; DB01294; Bismuth subsalicylate. DR DrugBank; DB09223; Blonanserin. DR DrugBank; DB00083; Botulinum toxin type A. DR DrugBank; DB01222; Budesonide. DR DrugBank; DB15248; Bulevirtide. DR DrugBank; DB00490; Buspirone. DR DrugBank; DB00237; Butabarbital. DR DrugBank; DB11148; Butamben. DR DrugBank; DB11751; Cabotegravir. DR DrugBank; DB11093; Calcium citrate. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR DrugBank; DB04690; Camptothecin. DR DrugBank; DB03600; Capric acid. DR DrugBank; DB01197; Captopril. DR DrugBank; DB01136; Carvedilol. DR DrugBank; DB00456; Cefalotin. DR DrugBank; DB01327; Cefazolin. DR DrugBank; DB14879; Cefiderocol. DR DrugBank; DB00274; Cefmetazole. DR DrugBank; DB01328; Cefonicid. DR DrugBank; DB01329; Cefoperazone. DR DrugBank; DB00493; Cefotaxime. DR DrugBank; DB01330; Cefotetan. DR DrugBank; DB00430; Cefpiramide. DR DrugBank; DB00438; Ceftazidime. DR DrugBank; DB01212; Ceftriaxone. DR DrugBank; DB06119; Cenobamate. DR DrugBank; DB00567; Cephalexin. DR DrugBank; DB07565; Chloramphenicol succinate. DR DrugBank; DB08936; Chlorcyclizine. DR DrugBank; DB00878; Chlorhexidine. DR DrugBank; DB00608; Chloroquine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB09093; Chlortetracycline. DR DrugBank; DB00310; Chlorthalidone. DR DrugBank; DB00501; Cimetidine. DR DrugBank; DB00568; Cinnarizine. DR DrugBank; DB00537; Ciprofloxacin. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB01013; Clobetasol propionate. DR DrugBank; DB00845; Clofazimine. DR DrugBank; DB01242; Clomipramine. DR DrugBank; DB01068; Clonazepam. DR DrugBank; DB00575; Clonidine. DR DrugBank; DB00758; Clopidogrel. DR DrugBank; DB01147; Cloxacillin. DR DrugBank; DB15534; Colchiceine. DR DrugBank; DB01394; Colchicine. DR DrugBank; DB00286; Conjugated estrogens. DR DrugBank; DB12483; Copanlisib. DR DrugBank; DB09130; Copper. DR DrugBank; DB01380; Cortisone acetate. DR DrugBank; DB08865; Crizotinib. DR DrugBank; DB11134; Cupric oxide. DR DrugBank; DB06778; Cupric sulfate. DR DrugBank; DB01176; Cyclizine. DR DrugBank; DB00924; Cyclobenzaprine. DR DrugBank; DB00434; Cyproheptadine. DR DrugBank; DB00847; Cysteamine. DR DrugBank; DB01914; D-glucose. DR DrugBank; DB06695; Dabigatran etexilate. DR DrugBank; DB08912; Dabrafenib. DR DrugBank; DB11963; Dacomitinib. DR DrugBank; DB04816; Dantron. DR DrugBank; DB00080; Daptomycin. DR DrugBank; DB12941; Darolutamide. DR DrugBank; DB01264; Darunavir. DR DrugBank; DB11943; Delafloxacin. DR DrugBank; DB11637; Delamanid. DR DrugBank; DB01189; Desflurane. DR DrugBank; DB00304; Desogestrel. DR DrugBank; DB01234; Dexamethasone. DR DrugBank; DB14649; Dexamethasone acetate. DR DrugBank; DB09213; Dexibuprofen. DR DrugBank; DB00829; Diazepam. DR DrugBank; DB11397; Dichlorvos. DR DrugBank; DB00586; Diclofenac. DR DrugBank; DB00485; Dicloxacillin. DR DrugBank; DB00266; Dicoumarol. DR DrugBank; DB00900; Didanosine. DR DrugBank; DB00861; Diflunisal. DR DrugBank; DB01396; Digitoxin. DR DrugBank; DB00343; Diltiazem. DR DrugBank; DB08995; Diosmin. DR DrugBank; DB08930; Dolutegravir. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB00997; Doxorubicin. DR DrugBank; DB00254; Doxycycline. DR DrugBank; DB00366; Doxylamine. DR DrugBank; DB04855; Dronedarone. DR DrugBank; DB00476; Duloxetine. DR DrugBank; DB01126; Dutasteride. DR DrugBank; DB01057; Echothiophate. DR DrugBank; DB12243; Edaravone. DR DrugBank; DB13421; Edoxudine. DR DrugBank; DB00625; Efavirenz. DR DrugBank; DB15444; Elexacaftor. DR DrugBank; DB00879; Emtricitabine. DR DrugBank; DB00584; Enalapril. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB08899; Enzalutamide. DR DrugBank; DB01364; Ephedrine. DR DrugBank; DB00530; Erlotinib. DR DrugBank; DB00303; Ertapenem. DR DrugBank; DB11827; Ertugliflozin. DR DrugBank; DB12235; Estetrol. DR DrugBank; DB00783; Estradiol. DR DrugBank; DB13952; Estradiol acetate. DR DrugBank; DB13953; Estradiol benzoate. DR DrugBank; DB13954; Estradiol cypionate. DR DrugBank; DB13955; Estradiol dienanthate. DR DrugBank; DB13956; Estradiol valerate. DR DrugBank; DB00655; Estrone. DR DrugBank; DB04574; Estrone sulfate. DR DrugBank; DB00903; Etacrynic acid. DR DrugBank; DB00977; Ethinylestradiol. DR DrugBank; DB00749; Etodolac. DR DrugBank; DB00294; Etonogestrel. DR DrugBank; DB01276; Exenatide. DR DrugBank; DB12466; Favipiravir. DR DrugBank; DB04854; Febuxostat. DR DrugBank; DB01039; Fenofibrate. DR DrugBank; DB00573; Fenoprofen. DR DrugBank; DB00813; Fentanyl. DR DrugBank; DB00950; Fexofenadine. DR DrugBank; DB16165; Finerenone. DR DrugBank; DB01195; Flecainide. DR DrugBank; DB00687; Fludrocortisone. DR DrugBank; DB15690; Fluoroestradiol F-18. DR DrugBank; DB00544; Fluorouracil. DR DrugBank; DB00472; Fluoxetine. DR DrugBank; DB00712; Flurbiprofen. DR DrugBank; DB00983; Formoterol. DR DrugBank; DB01320; Fosphenytoin. DR DrugBank; DB06716; Fospropofol. DR DrugBank; DB11796; Fostemsavir. DR DrugBank; DB00695; Furosemide. DR DrugBank; DB15149; Futibatinib. DR DrugBank; DB00743; Gadobenic acid. DR DrugBank; DB06705; Gadofosveset trisodium. DR DrugBank; DB01044; Gatifloxacin. DR DrugBank; DB00317; Gefitinib. DR DrugBank; DB01241; Gemfibrozil. DR DrugBank; DB12141; Gilteritinib. DR DrugBank; DB11978; Glasdegib. DR DrugBank; DB01120; Gliclazide. DR DrugBank; DB01067; Glipizide. DR DrugBank; DB01016; Glyburide. DR DrugBank; DB00986; Glycopyrronium. DR DrugBank; DB13751; Glycyrrhizic acid. DR DrugBank; DB04539; Glyphosate. DR DrugBank; DB12836; Grapiprant. DR DrugBank; DB11575; Grazoprevir. DR DrugBank; DB11359; Guaiacol. DR DrugBank; DB01159; Halothane. DR DrugBank; DB14999; Human interferon beta. DR DrugBank; DB00070; Hyaluronidase (ovine). DR DrugBank; DB01275; Hydralazine. DR DrugBank; DB00999; Hydrochlorothiazide. DR DrugBank; DB00774; Hydroflumethiazide. DR DrugBank; DB00327; Hydromorphone. DR DrugBank; DB09526; Hydroquinone. DR DrugBank; DB01611; Hydroxychloroquine. DR DrugBank; DB00557; Hydroxyzine. DR DrugBank; DB13014; Hypericin. DR DrugBank; DB12471; Ibrexafungerp. DR DrugBank; DB09053; Ibrutinib. DR DrugBank; DB01050; Ibuprofen. DR DrugBank; DB00159; Icosapent. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB09262; Imidafenacin. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB00808; Indapamide. DR DrugBank; DB00328; Indomethacin. DR DrugBank; DB07992; Indoxyl sulfate. DR DrugBank; DB09564; Insulin degludec. DR DrugBank; DB01307; Insulin detemir. DR DrugBank; DB05382; Iodine. DR DrugBank; DB04711; Iodipamide. DR DrugBank; DB09333; Iopodic acid. DR DrugBank; DB00332; Ipratropium. DR DrugBank; DB01029; Irbesartan. DR DrugBank; DB00762; Irinotecan. DR DrugBank; DB00753; Isoflurane. DR DrugBank; DB00677; Isoflurophate. DR DrugBank; DB00951; Isoniazid. DR DrugBank; DB01064; Isoprenaline. DR DrugBank; DB00982; Isotretinoin. DR DrugBank; DB11757; Istradefylline. DR DrugBank; DB08820; Ivacaftor. DR DrugBank; DB01587; Ketazolam. DR DrugBank; DB01026; Ketoconazole. DR DrugBank; DB01009; Ketoprofen. DR DrugBank; DB00598; Labetalol. DR DrugBank; DB09236; Lacidipine. DR DrugBank; DB00709; Lamivudine. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB03017; Lauric acid. DR DrugBank; DB01006; Letrozole. DR DrugBank; DB09237; Levamlodipine. DR DrugBank; DB06282; Levocetirizine. DR DrugBank; DB01235; Levodopa. DR DrugBank; DB01137; Levofloxacin. DR DrugBank; DB00451; Levothyroxine. DR DrugBank; DB00601; Linezolid. DR DrugBank; DB17083; Linzagolix. DR DrugBank; DB00279; Liothyronine. DR DrugBank; DB01583; Liotrix. DR DrugBank; DB06655; Liraglutide. DR DrugBank; DB01601; Lopinavir. DR DrugBank; DB09195; Lorpiprazole. DR DrugBank; DB00678; Losartan. DR DrugBank; DB00227; Lovastatin. DR DrugBank; DB09280; Lumacaftor. DR DrugBank; DB15935; Lumasiran. DR DrugBank; DB12674; Lurbinectedin. DR DrugBank; DB00137; Lutein. DR DrugBank; DB08932; Macitentan. DR DrugBank; DB14513; Magnesium. DR DrugBank; DB01397; Magnesium salicylate. DR DrugBank; DB06796; Mangafodipir. DR DrugBank; DB06234; Maribavir. DR DrugBank; DB00737; Meclizine. DR DrugBank; DB13959; Medium-chain triglycerides. DR DrugBank; DB09124; Medrogestone. DR DrugBank; DB00603; Medroxyprogesterone acetate. DR DrugBank; DB00784; Mefenamic acid. DR DrugBank; DB00814; Meloxicam. DR DrugBank; DB00454; Meperidine. DR DrugBank; DB09383; Meprednisone. DR DrugBank; DB00931; Metacycline. DR DrugBank; DB00333; Methadone. DR DrugBank; DB00563; Methotrexate. DR DrugBank; DB00968; Methyldopa. DR DrugBank; DB09241; Methylene blue. DR DrugBank; DB00959; Methylprednisolone. DR DrugBank; DB06710; Methyltestosterone. DR DrugBank; DB00264; Metoprolol. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB08893; Mirabegron. DR DrugBank; DB00295; Morphine. DR DrugBank; DB01024; Mycophenolic acid. DR DrugBank; DB08231; Myristic acid. DR DrugBank; DB00461; Nabumetone. DR DrugBank; DB00607; Nafcillin. DR DrugBank; DB01183; Naloxone. DR DrugBank; DB00788; Naproxen. DR DrugBank; DB00731; Nateglinide. DR DrugBank; DB04861; Nebivolol. DR DrugBank; DB00220; Nelfinavir. DR DrugBank; DB11828; Neratinib. DR DrugBank; DB00238; Nevirapine. DR DrugBank; DB01115; Nifedipine. DR DrugBank; DB11820; Nifurtimox. DR DrugBank; DB09079; Nintedanib. DR DrugBank; DB11793; Niraparib. DR DrugBank; DB06713; Norelgestromin. DR DrugBank; DB00717; Norethisterone. DR DrugBank; DB00957; Norgestimate. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB00104; Octreotide. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB09074; Olaparib. DR DrugBank; DB04224; Oleic Acid. DR DrugBank; DB00768; Olopatadine. DR DrugBank; DB12455; Omadacycline. DR DrugBank; DB11130; Opium. DR DrugBank; DB04911; Oritavancin. DR DrugBank; DB01083; Orlistat. DR DrugBank; DB13310; Ormeloxifene. DR DrugBank; DB01173; Orphenadrine. DR DrugBank; DB00842; Oxazepam. DR DrugBank; DB00776; Oxcarbazepine. DR DrugBank; DB01062; Oxybutynin. DR DrugBank; DB00497; Oxycodone. DR DrugBank; DB06412; Oxymetholone. DR DrugBank; DB03585; Oxyphenbutazone. DR DrugBank; DB00595; Oxytetracycline. DR DrugBank; DB15575; Padeliporfin. DR DrugBank; DB09073; Palbociclib. DR DrugBank; DB03796; Palmitic Acid. DR DrugBank; DB13967; Patent Blue. DR DrugBank; DB14582; Patisiran. DR DrugBank; DB00642; Pemetrexed. DR DrugBank; DB00850; Perphenazine. DR DrugBank; DB12978; Pexidartinib. DR DrugBank; DB01619; Phenindamine. DR DrugBank; DB03255; Phenol. DR DrugBank; DB00946; Phenprocoumon. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB01132; Pioglitazone. DR DrugBank; DB01621; Pipotiazine. DR DrugBank; DB04951; Pirfenidone. DR DrugBank; DB00554; Piroxicam. DR DrugBank; DB08860; Pitavastatin. DR DrugBank; DB11642; Pitolisant. DR DrugBank; DB01324; Polythiazide. DR DrugBank; DB09087; Potassium alum. DR DrugBank; DB09418; Potassium perchlorate. DR DrugBank; DB06813; Pralatrexate. DR DrugBank; DB13514; Pranoprofen. DR DrugBank; DB06209; Prasugrel. DR DrugBank; DB00860; Prednisolone. DR DrugBank; DB15566; Prednisolone acetate. DR DrugBank; DB14631; Prednisolone phosphate. DR DrugBank; DB00635; Prednisone. DR DrugBank; DB01032; Probenecid. DR DrugBank; DB01069; Promethazine. DR DrugBank; DB09348; Propiolactone. DR DrugBank; DB00818; Propofol. DR DrugBank; DB00571; Propranolol. DR DrugBank; DB06480; Prucalopride. DR DrugBank; DB00852; Pseudoephedrine. DR DrugBank; DB00165; Pyridoxine. DR DrugBank; DB04216; Quercetin. DR DrugBank; DB00881; Quinapril. DR DrugBank; DB00908; Quinidine. DR DrugBank; DB08735; R,S-Warfarin alcohol. DR DrugBank; DB00481; Raloxifene. DR DrugBank; DB11853; Relugolix. DR DrugBank; DB12404; Remimazolam. DR DrugBank; DB00912; Repaglinide. DR DrugBank; DB02709; Resveratrol. DR DrugBank; DB11855; Revefenacin. DR DrugBank; DB01045; Rifampicin. DR DrugBank; DB11753; Rifamycin. DR DrugBank; DB08864; Rilpivirine. DR DrugBank; DB08931; Riociguat. DR DrugBank; DB14840; Ripretinib. DR DrugBank; DB15305; Risdiplam. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB11182; Rose bengal. DR DrugBank; DB00412; Rosiglitazone. DR DrugBank; DB01098; Rosuvastatin. DR DrugBank; DB04847; Roxadustat. DR DrugBank; DB06201; Rufinamide. DR DrugBank; DB08877; Ruxolitinib. DR DrugBank; DB08736; S,R-Warfarin alcohol. DR DrugBank; DB00936; Salicylic acid. DR DrugBank; DB00938; Salmeterol. DR DrugBank; DB01232; Saquinavir. DR DrugBank; DB11689; Selumetinib. DR DrugBank; DB13928; Semaglutide. DR DrugBank; DB01104; Sertraline. DR DrugBank; DB01236; Sevoflurane. DR DrugBank; DB12965; Silver. DR DrugBank; DB06290; Simeprevir. DR DrugBank; DB00877; Sirolimus. DR DrugBank; DB00815; Sodium lauryl sulfate. DR DrugBank; DB15093; Somapacitan. DR DrugBank; DB00421; Spironolactone. DR DrugBank; DB00649; Stavudine. DR DrugBank; DB03193; Stearic acid. DR DrugBank; DB06150; Sulfadimethoxine. DR DrugBank; DB01581; Sulfamerazine. DR DrugBank; DB01582; Sulfamethazine. DR DrugBank; DB00576; Sulfamethizole. DR DrugBank; DB01015; Sulfamethoxazole. DR DrugBank; DB00795; Sulfasalazine. DR DrugBank; DB00605; Sulindac. DR DrugBank; DB00391; Sulpiride. DR DrugBank; DB00870; Suprofen. DR DrugBank; DB00864; Tacrolimus. DR DrugBank; DB00675; Tamoxifen. DR DrugBank; DB05134; Tanespimycin. DR DrugBank; DB09139; Technetium Tc-99m oxidronate. DR DrugBank; DB05521; Telaprevir. DR DrugBank; DB00853; Temozolomide. DR DrugBank; DB14126; Tenofovir. DR DrugBank; DB09299; Tenofovir alafenamide. DR DrugBank; DB15133; Tepotinib. DR DrugBank; DB00857; Terbinafine. DR DrugBank; DB00342; Terfenadine. DR DrugBank; DB00624; Testosterone. DR DrugBank; DB13943; Testosterone cypionate. DR DrugBank; DB13944; Testosterone enanthate. DR DrugBank; DB01420; Testosterone propionate. DR DrugBank; DB13946; Testosterone undecanoate. DR DrugBank; DB00759; Tetracycline. DR DrugBank; DB00152; Thiamine. DR DrugBank; DB11590; Thimerosal. DR DrugBank; DB01622; Thioproperazine. DR DrugBank; DB01623; Thiothixene. DR DrugBank; DB09100; Thyroid, porcine. DR DrugBank; DB09070; Tibolone. DR DrugBank; DB08816; Ticagrelor. DR DrugBank; DB01133; Tiludronic acid. DR DrugBank; DB15171; Tirzepatide. DR DrugBank; DB11800; Tivozanib. DR DrugBank; DB01056; Tocainide. DR DrugBank; DB08895; Tofacitinib. DR DrugBank; DB01124; Tolbutamide. DR DrugBank; DB00500; Tolmetin. DR DrugBank; DB00273; Topiramate. DR DrugBank; DB01685; Topiroxostat. DR DrugBank; DB00214; Torasemide. DR DrugBank; DB00755; Tretinoin. DR DrugBank; DB00620; Triamcinolone. DR DrugBank; DB00432; Trifluridine. DR DrugBank; DB08814; Triflusal. DR DrugBank; DB11677; Triheptanoin. DR DrugBank; DB00376; Trihexyphenidyl. DR DrugBank; DB09069; Trimetazidine. DR DrugBank; DB00792; Tripelennamine. DR DrugBank; DB00427; Triprolidine. DR DrugBank; DB08867; Ulipristal. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB00512; Vancomycin. DR DrugBank; DB05294; Vandetanib. DR DrugBank; DB08881; Vemurafenib. DR DrugBank; DB00661; Verapamil. DR DrugBank; DB15456; Vericiguat. DR DrugBank; DB11641; Vinflunine. DR DrugBank; DB08828; Vismodegib. DR DrugBank; DB00162; Vitamin A. DR DrugBank; DB11739; Vonoprazan. DR DrugBank; DB16699; Vutrisiran. DR DrugBank; DB00682; Warfarin. DR DrugBank; DB00943; Zalcitabine. DR DrugBank; DB00495; Zidovudine. DR DrugBank; DB00744; Zileuton. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB04828; Zomepirac. DR DrugCentral; P02768; -. DR Allergome; 763; Hom s HSA. DR CarbonylDB; P02768; -. DR GlyConnect; 559; 2 N-Linked glycans (2 sites), 3 O-Linked glycans (2 sites). DR GlyCosmos; P02768; 32 sites, 10 glycans. DR GlyGen; P02768; 10 sites, 2 N-linked glycans (1 site), 7 O-linked glycans (9 sites). DR iPTMnet; P02768; -. DR MetOSite; P02768; -. DR PhosphoSitePlus; P02768; -. DR SwissPalm; P02768; -. DR BioMuta; ALB; -. DR DMDM; 113576; -. DR DOSAC-COBS-2DPAGE; P02768; -. DR OGP; P02768; -. DR REPRODUCTION-2DPAGE; IPI00384697; -. DR REPRODUCTION-2DPAGE; IPI00745872; -. DR REPRODUCTION-2DPAGE; P02768; -. DR CPTAC; non-CPTAC-1160; -. DR jPOST; P02768; -. DR MassIVE; P02768; -. DR PaxDb; 9606-ENSP00000295897; -. DR PeptideAtlas; P02768; -. DR PRIDE; P02768; -. DR ProteomicsDB; 51587; -. [P02768-1] DR ProteomicsDB; 51588; -. [P02768-2] DR ProteomicsDB; 70582; -. DR ABCD; P02768; 105 sequenced antibodies. DR Antibodypedia; 3342; 3472 antibodies from 52 providers. DR DNASU; 213; -. DR Ensembl; ENST00000295897.9; ENSP00000295897.4; ENSG00000163631.18. [P02768-1] DR GeneID; 213; -. DR KEGG; hsa:213; -. DR MANE-Select; ENST00000295897.9; ENSP00000295897.4; NM_000477.7; NP_000468.1. DR UCSC; uc003hgs.5; human. [P02768-1] DR UCSC; uc062xfr.1; human. DR AGR; HGNC:399; -. DR CTD; 213; -. DR DisGeNET; 213; -. DR GeneCards; ALB; -. DR HGNC; HGNC:399; ALB. DR HPA; ENSG00000163631; Tissue enriched (liver). DR MalaCards; ALB; -. DR MIM; 103600; gene. DR MIM; 615999; phenotype. DR MIM; 616000; phenotype. DR neXtProt; NX_P02768; -. DR OpenTargets; ENSG00000163631; -. DR Orphanet; 86816; Congenital analbuminemia. DR Orphanet; 276271; NON RARE IN EUROPE: Familial dysalbuminemic hyperthyroxinemia. DR PharmGKB; PA24690; -. DR VEuPathDB; HostDB:ENSG00000163631; -. DR eggNOG; ENOG502R7EA; Eukaryota. DR GeneTree; ENSGT00390000000113; -. DR InParanoid; P02768; -. DR OMA; ADPHACY; -. DR OrthoDB; 5196468at2759; -. DR PhylomeDB; P02768; -. DR TreeFam; TF335561; -. DR PathwayCommons; P02768; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-159418; Recycling of bile acids and salts. DR Reactome; R-HSA-189451; Heme biosynthesis. DR Reactome; R-HSA-189483; Heme degradation. DR Reactome; R-HSA-2168880; Scavenging of heme from plasma. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR Reactome; R-HSA-8964058; HDL remodeling. DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. DR Reactome; R-HSA-9749641; Aspirin ADME. DR Reactome; R-HSA-9757110; Prednisone ADME. DR Reactome; R-HSA-9793528; Ciprofloxacin ADME. DR SignaLink; P02768; -. DR SIGNOR; P02768; -. DR BioGRID-ORCS; 213; 8 hits in 1149 CRISPR screens. DR ChiTaRS; ALB; human. DR EvolutionaryTrace; P02768; -. DR GeneWiki; Serum_albumin; -. DR GenomeRNAi; 213; -. DR Pharos; P02768; Tchem. DR PRO; PR:P02768; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P02768; Protein. DR Bgee; ENSG00000163631; Expressed in liver and 114 other cell types or tissues. DR ExpressionAtlas; P02768; baseline and differential. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0016209; F:antioxidant activity; NAS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:1903981; F:enterobactin binding; IDA:UniProtKB. DR GO; GO:0140272; F:exogenous protein binding; IDA:UniProtKB. DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:BHF-UCL. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB. DR GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB. DR GO; GO:0072732; P:cellular response to calcium ion starvation; IDA:UniProtKB. DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB. DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IDA:UniProtKB. DR CDD; cd00015; ALBUMIN; 3. DR Gene3D; 1.10.246.10; -; 6. DR InterPro; IPR000264; ALB/AFP/VDB. DR InterPro; IPR020858; Serum_albumin-like. DR InterPro; IPR021177; Serum_albumin/AFP/Afamin. DR InterPro; IPR020857; Serum_albumin_CS. DR InterPro; IPR014760; Serum_albumin_N. DR PANTHER; PTHR11385:SF15; ALBUMIN; 1. DR PANTHER; PTHR11385; SERUM ALBUMIN-RELATED; 1. DR Pfam; PF00273; Serum_albumin; 3. DR PIRSF; PIRSF002520; Serum_albumin_subgroup; 1. DR PRINTS; PR00802; SERUMALBUMIN. DR SMART; SM00103; ALBUMIN; 3. DR SUPFAM; SSF48552; Serum albumin-like; 3. DR PROSITE; PS00212; ALBUMIN_1; 3. DR PROSITE; PS51438; ALBUMIN_2; 3. DR SWISS-2DPAGE; P02768; -. DR UCD-2DPAGE; P02768; -. DR Genevisible; P02768; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; KW Cleavage on pair of basic residues; Copper; Direct protein sequencing; KW Disease variant; Disulfide bond; Glycation; Glycoprotein; Lipid-binding; KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat; KW Secreted; Signal; Zinc. FT SIGNAL 1..18 FT PROPEP 19..24 FT /id="PRO_0000001067" FT CHAIN 25..609 FT /note="Albumin" FT /id="PRO_0000001068" FT DOMAIN 19..210 FT /note="Albumin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT DOMAIN 211..403 FT /note="Albumin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT DOMAIN 404..601 FT /note="Albumin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT BINDING 27 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000250|UniProtKB:P02770" FT BINDING 30 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P02769" FT BINDING 37 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P02769" FT BINDING 91 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28567254, FT ECO:0007744|PDB:5IJF" FT BINDING 264 FT /ligand="bilirubin IXalpha" FT /ligand_id="ChEBI:CHEBI:57977" FT /evidence="ECO:0000269|PubMed:656055" FT BINDING 268 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P02769" FT BINDING 271 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28567254, FT ECO:0007744|PDB:5IJF" FT BINDING 273 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P02769" FT BINDING 273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:28567254, FT ECO:0007744|PDB:5IJF" FT BINDING 276 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P02769" FT BINDING 279 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P02769" FT BINDING 283 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P02769" FT SITE 28 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 44 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 65 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 88 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 97 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 117 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 130 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 160 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 183 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 198 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 205 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 214 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 219 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 223 FT /note="Aspirin-acetylated lysine" FT SITE 229 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 236 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 264 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 286 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 298 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 310 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 383 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 396 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 413 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 426 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 438 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 456 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 460 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 490 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 499 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 524 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 543 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 548 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 562 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 565 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 581 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 584 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 588 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT SITE 598 FT /note="Not glycated" FT /evidence="ECO:0000269|PubMed:15047055" FT MOD_RES 29 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 82 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569" FT MOD_RES 89 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039, FT ECO:0007744|PubMed:24275569" FT MOD_RES 107 FT /note="Phosphothreonine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 229 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P07724" FT MOD_RES 297 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07724" FT MOD_RES 443 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 444 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 446 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 460 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P07724" FT MOD_RES 513 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 543 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P07724" FT MOD_RES 558 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 588 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P07724" FT CARBOHYD 36 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:3759977" FT CARBOHYD 75 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 161 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 186 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 223 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:3759977, FT ECO:0000269|PubMed:6853480" FT CARBOHYD 249 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 257 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:15047055, FT ECO:0000269|PubMed:3759977" FT CARBOHYD 300 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 305 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:3759977" FT CARBOHYD 337 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 341 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:3759977" FT CARBOHYD 342 FT /note="N-linked (GlcNAc...) asparagine; in variant Redhill" FT /id="CAR_000226" FT CARBOHYD 347 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 375 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:15047055, FT ECO:0000269|PubMed:3759977" FT CARBOHYD 402 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 437 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 463 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:3759977" FT CARBOHYD 468 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 518 FT /note="N-linked (GlcNAc...) asparagine; in variant FT Casebrook" FT /id="CAR_000069" FT CARBOHYD 549 FT /note="N-linked (Glc) (glycation) lysine" FT /evidence="ECO:0000269|PubMed:15047055, FT ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, FT ECO:0000269|PubMed:6853480" FT CARBOHYD 558 FT /note="N-linked (Glc) (glycation) lysine; alternate" FT /evidence="ECO:0000269|PubMed:3759977" FT CARBOHYD 560 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 569 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT CARBOHYD 597 FT /note="N-linked (Glc) (glycation) lysine; in vitro" FT /evidence="ECO:0000269|PubMed:15047055" FT DISULFID 77..86 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 99..115 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 114..125 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 148..193 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 192..201 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 224..270 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 269..277 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 289..303 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 302..313 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 340..385 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 384..393 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 416..462 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 461..472 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 485..501 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 500..511 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 538..583 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT DISULFID 582..591 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769, FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28, FT ECO:0007744|PDB:5IJF" FT VAR_SEQ 43..234 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.9" FT /id="VSP_021275" FT VAR_SEQ 164..376 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_057389" FT VARIANT 23 FT /note="R -> C (in Redhill/Malmo-I/Tradate; associated in FT cis with T-344 in Redhill; dbSNP:rs80008208)" FT /evidence="ECO:0000269|PubMed:1518850" FT /id="VAR_000499" FT VARIANT 23 FT /note="R -> H (in Fukuoka-2/Lille/Taipei/Varese/Komagome-3; FT dbSNP:rs72552709)" FT /evidence="ECO:0000269|PubMed:1946412, FT ECO:0000269|PubMed:2247440, ECO:0000269|PubMed:2911589" FT /id="VAR_000500" FT VARIANT 24 FT /note="R -> L (in Jaffna; dbSNP:rs74821926)" FT /id="VAR_000501" FT VARIANT 24 FT /note="R -> P (in Takefu/Honolulu-1; dbSNP:rs74821926)" FT /evidence="ECO:0000269|PubMed:2404284" FT /id="VAR_000502" FT VARIANT 24 FT /note="R -> Q (in Christchurch/Honolulu-2; FT dbSNP:rs74821926)" FT /evidence="ECO:0000269|PubMed:2404284, FT ECO:0000269|PubMed:2762316, ECO:0000269|PubMed:2911589" FT /id="VAR_000503" FT VARIANT 25 FT /note="D -> V (in Bleinheim/Iowa city-2; dbSNP:rs75353611)" FT /evidence="ECO:0000269|PubMed:1946412" FT /id="VAR_000504" FT VARIANT 27 FT /note="H -> Q (in Nagasaki-3; dbSNP:rs76285851)" FT /id="VAR_000505" FT VARIANT 27 FT /note="H -> Y (in Larino; dbSNP:rs141733599)" FT /evidence="ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:8022807" FT /id="VAR_000506" FT VARIANT 73 FT /note="F -> Y" FT /evidence="ECO:0000269|PubMed:11680902" FT /id="VAR_010657" FT VARIANT 84 FT /note="E -> K (in Torino; dbSNP:rs77050410)" FT /evidence="ECO:0000269|PubMed:2247440" FT /id="VAR_000507" FT VARIANT 87 FT /note="D -> N (in Malmo-95/Dalakarlia; dbSNP:rs78574148)" FT /evidence="ECO:0000269|PubMed:1518850" FT /id="VAR_000508" FT VARIANT 90 FT /note="L -> P (in FDAH; dbSNP:rs77892378)" FT /evidence="ECO:0000269|PubMed:9589637" FT /id="VAR_013011" FT VARIANT 106 FT /note="E -> K (in Vibo Valentia; dbSNP:rs80296402)" FT /evidence="ECO:0000269|PubMed:2247440" FT /id="VAR_000509" FT VARIANT 121 FT /note="E -> G" FT /evidence="ECO:0000269|PubMed:6275391" FT /id="VAR_014290" FT VARIANT 138 FT /note="R -> G (in Yanomama-2; dbSNP:rs77238412)" FT /id="VAR_000510" FT VARIANT 143 FT /note="E -> K (in Nagoya; dbSNP:rs75522063)" FT /evidence="ECO:0000269|PubMed:2404284" FT /id="VAR_000511" FT VARIANT 146 FT /note="V -> E (in Tregasio; dbSNP:rs77752336)" FT /id="VAR_013012" FT VARIANT 152 FT /note="H -> R (in Komagome-2; dbSNP:rs80095457)" FT /evidence="ECO:0000269|PubMed:1946412" FT /id="VAR_000512" FT VARIANT 201 FT /note="C -> F (in Hawkes bay; dbSNP:rs77656691)" FT /evidence="ECO:0000269|PubMed:8347685" FT /id="VAR_000513" FT VARIANT 215 FT /note="A -> T (in dbSNP:rs3210154)" FT /id="VAR_014291" FT VARIANT 215 FT /note="A -> V (in dbSNP:rs3204504)" FT /id="VAR_014292" FT VARIANT 220 FT /note="Q -> L (in dbSNP:rs3210163)" FT /id="VAR_014293" FT VARIANT 242 FT /note="R -> H (in FDAH; dbSNP:rs75002628)" FT /evidence="ECO:0000269|PubMed:7852505, FT ECO:0000269|PubMed:8048949" FT /id="VAR_000514" FT VARIANT 242 FT /note="R -> P (in FDAH; dbSNP:rs75002628)" FT /evidence="ECO:0000269|PubMed:9329347" FT /id="VAR_013013" FT VARIANT 249 FT /note="K -> Q (in Tradate-2; dbSNP:rs79804069)" FT /evidence="ECO:0000269|PubMed:8022807" FT /id="VAR_000515" FT VARIANT 264 FT /note="K -> E (in Herborn; dbSNP:rs79377490)" FT /evidence="ECO:0000269|PubMed:8513793" FT /id="VAR_000516" FT VARIANT 292 FT /note="Q -> R (in Malmo-10; dbSNP:rs80002911)" FT /evidence="ECO:0000269|PubMed:1518850" FT /id="VAR_000517" FT VARIANT 293 FT /note="D -> G (in Nagasaki-1; dbSNP:rs79744198)" FT /evidence="ECO:0000269|PubMed:2762316" FT /id="VAR_000518" FT VARIANT 300 FT /note="K -> N (in Caserta; dbSNP:rs74718349)" FT /evidence="ECO:0000269|PubMed:8022807" FT /id="VAR_000519" FT VARIANT 337 FT /note="K -> N (in Canterbury/New FT Guinea/Tagliacozzo/Cuneo/Cooperstown; dbSNP:rs72552710)" FT /evidence="ECO:0000269|PubMed:2404284, FT ECO:0000269|PubMed:2911589, ECO:0000269|PubMed:3828358" FT /id="VAR_000520" FT VARIANT 338 FT /note="D -> G (in Bergamo; dbSNP:rs76242087)" FT /id="VAR_013014" FT VARIANT 338 FT /note="D -> V (in Brest; dbSNP:rs76242087)" FT /id="VAR_013015" FT VARIANT 342 FT /note="N -> K (in Malmo-47; dbSNP:rs77544362)" FT /evidence="ECO:0000269|PubMed:1518850" FT /id="VAR_000521" FT VARIANT 344 FT /note="A -> T (in Redhill; associated in cis with C-23; FT dbSNP:rs78953271)" FT /id="VAR_000522" FT VARIANT 345 FT /note="E -> K (in Roma; dbSNP:rs72552711)" FT /id="VAR_000523" FT VARIANT 357 FT /note="E -> K (in Sondrio; dbSNP:rs77354753)" FT /evidence="ECO:0000269|PubMed:1347703" FT /id="VAR_000524" FT VARIANT 378 FT /note="E -> K (in Hiroshima-1; dbSNP:rs76593094)" FT /evidence="ECO:0000269|PubMed:2762316, ECO:0000269|Ref.5" FT /id="VAR_000525" FT VARIANT 382 FT /note="E -> K (in Coari I/Porto Alegre; dbSNP:rs75791663)" FT /id="VAR_000526" FT VARIANT 383 FT /note="K -> N (in Trieste; dbSNP:rs75069738)" FT /id="VAR_013016" FT VARIANT 389 FT /note="D -> H (in Parklands; dbSNP:rs77187142)" FT /id="VAR_000527" FT VARIANT 389 FT /note="D -> V (in Iowa city-1; dbSNP:rs78538497)" FT /evidence="ECO:0000269|PubMed:1946412" FT /id="VAR_000528" FT VARIANT 396 FT /note="K -> E (in Naskapi/Mersin/Komagome-1; FT dbSNP:rs78166690)" FT /evidence="ECO:0000269|PubMed:1946412, FT ECO:0000269|PubMed:3474609, ECO:0000269|PubMed:3479777" FT /id="VAR_000529" FT VARIANT 399 FT /note="D -> N (in Nagasaki-2; dbSNP:rs77514449)" FT /evidence="ECO:0000269|PubMed:3479777" FT /id="VAR_000530" FT VARIANT 400 FT /note="E -> K (in Tochigi; dbSNP:rs79047363)" FT /evidence="ECO:0000269|PubMed:2762316" FT /id="VAR_000531" FT VARIANT 400 FT /note="E -> Q (in Malmo-5; dbSNP:rs79047363)" FT /evidence="ECO:0000269|PubMed:1518850" FT /id="VAR_000532" FT VARIANT 406 FT /note="E -> K (in Hiroshima-2; dbSNP:rs76483862)" FT /evidence="ECO:0000269|PubMed:2762316" FT /id="VAR_000533" FT VARIANT 420 FT /note="E -> K" FT /evidence="ECO:0000269|PubMed:6171778" FT /id="VAR_014294" FT VARIANT 434 FT /note="R -> C (in Liprizzi; dbSNP:rs78575701)" FT /id="VAR_013017" FT VARIANT 490 FT /note="K -> E (in dbSNP:rs1063469)" FT /id="VAR_014295" FT VARIANT 503 FT /note="E -> K (in Dublin; dbSNP:rs80259813)" FT /id="VAR_000534" FT VARIANT 518 FT /note="D -> N (in Casebrook; dbSNP:rs75920790)" FT /evidence="ECO:0000269|PubMed:1859851" FT /id="VAR_000535" FT VARIANT 525 FT /note="E -> K (in Manaus-1/Adana/Lambadi/Vancouver; FT dbSNP:rs75523493)" FT /evidence="ECO:0000269|PubMed:2404284" FT /id="VAR_000536" FT VARIANT 529 FT /note="E -> K (in Ortonovo; dbSNP:rs74826639)" FT /evidence="ECO:0000269|PubMed:7902134" FT /id="VAR_000537" FT VARIANT 557 FT /note="V -> M (in Maddaloni; dbSNP:rs78284052)" FT /id="VAR_013018" FT VARIANT 560 FT /note="K -> E (in Castel di Sangro; dbSNP:rs77645174)" FT /id="VAR_000538" FT VARIANT 565 FT /note="K -> E (in Maku; dbSNP:rs80345158)" FT /evidence="ECO:0000269|PubMed:3479777" FT /id="VAR_000539" FT VARIANT 574 FT /note="D -> A (in Malmo-61; dbSNP:rs79738788)" FT /evidence="ECO:0000269|PubMed:1518850" FT /id="VAR_000541" FT VARIANT 574 FT /note="D -> G (in Mexico; dbSNP:rs79738788)" FT /evidence="ECO:0000269|PubMed:3474609" FT /id="VAR_000540" FT VARIANT 584 FT /note="K -> E (in Church bay; dbSNP:rs76671808)" FT /id="VAR_013019" FT VARIANT 587 FT /note="D -> N (in Fukuoka-1/Paris-2; dbSNP:rs76587671)" FT /evidence="ECO:0000269|PubMed:1347703, FT ECO:0000269|PubMed:2404284" FT /id="VAR_000542" FT VARIANT 589 FT /note="E -> K (in Osaka-1; dbSNP:rs75709682)" FT /evidence="ECO:0000269|PubMed:2404284" FT /id="VAR_000543" FT VARIANT 594 FT /note="E -> K (in Osaka-2/Phnom Phen/albumin B/Verona; FT dbSNP:rs79228041)" FT /evidence="ECO:0000269|PubMed:2404284, FT ECO:0000269|PubMed:2762316, ECO:0000269|PubMed:2911589" FT /id="VAR_000544" FT VARIANT 596..609 FT /note="GKKLVAASQAALGL -> PTMRIRERK (in Venezia)" FT /id="VAR_000547" FT VARIANT 597 FT /note="K -> E (in Gent/Milano Fast; dbSNP:rs80106970)" FT /id="VAR_000545" FT VARIANT 598 FT /note="K -> N (in Vanves; dbSNP:rs75738598)" FT /id="VAR_000546" FT VARIANT 599..609 FT /note="LVAASQAALGL -> TCCCKSSCLRLITSHLKASQPTMRIRERK (in FT Kenitra)" FT /id="VAR_012981" FT MUTAGEN 91 FT /note="H->A: Impairs metal binding." FT /evidence="ECO:0000269|PubMed:28567254" FT CONFLICT 55 FT /note="L -> P (in Ref. 11; CAH18185)" FT /evidence="ECO:0000305" FT CONFLICT 122 FT /note="R -> S (in Ref. 4; AAF01333)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="E -> Q (in Ref. 19; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 174 FT /note="Y -> L (in Ref. 24; AA sequence and 25; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 194 FT /note="Q -> E (in Ref. 19; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 327..332 FT /note="PSLAAD -> MFVLLC (in Ref. 10; AAF71067)" FT /evidence="ECO:0000305" FT CONFLICT 405 FT /note="V -> A (in Ref. 10; AAF71067)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="Q -> E (in Ref. 15; AAH14308)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="Q -> E (in Ref. 2; CAA23753)" FT /evidence="ECO:0000305" FT CONFLICT 466 FT /note="E -> G (in Ref. 4; AAF01333)" FT /evidence="ECO:0000305" FT CONFLICT 488..489 FT /note="HE -> EH (in Ref. 19; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 490 FT /note="K -> R (in Ref. 11; CAH18185)" FT /evidence="ECO:0000305" FT CONFLICT 525 FT /note="E -> Q (in Ref. 19; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 551 FT /note="T -> A (in Ref. 11; CAH18185)" FT /evidence="ECO:0000305" FT CONFLICT 560 FT /note="K -> R (in Ref. 11; CAH18185)" FT /evidence="ECO:0000305" FT CONFLICT 604 FT /note="Q -> R (in Ref. 5; AAN17825)" FT /evidence="ECO:0000305" FT HELIX 30..38 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 40..54 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:2BXH" FT HELIX 60..79 FT /evidence="ECO:0007829|PDB:6YG9" FT TURN 84..87 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 90..100 FT /evidence="ECO:0007829|PDB:6YG9" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:2BXH" FT HELIX 104..108 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 109..116 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:6A7P" FT HELIX 121..128 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:4N0F" FT HELIX 144..153 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 155..169 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:5ID7" FT HELIX 175..192 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 198..246 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:6EZQ" FT HELIX 252..271 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 274..289 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 290..294 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:5Z0B" FT HELIX 300..304 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 307..315 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 330..333 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:2BXP" FT HELIX 339..344 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 347..361 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:7WKZ" FT HELIX 367..384 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:1N5U" FT HELIX 390..394 FT /evidence="ECO:0007829|PDB:1N5U" FT TURN 397..401 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 402..419 FT /evidence="ECO:0007829|PDB:6YG9" FT TURN 420..422 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 423..438 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 440..442 FT /evidence="ECO:0007829|PDB:6EZQ" FT HELIX 444..461 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 462..464 FT /evidence="ECO:0007829|PDB:2BXH" FT TURN 466..468 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 469..490 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 495..502 FT /evidence="ECO:0007829|PDB:6YG9" FT TURN 505..507 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 508..513 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 519..521 FT /evidence="ECO:0007829|PDB:6R7S" FT HELIX 528..530 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 535..538 FT /evidence="ECO:0007829|PDB:6YG9" FT HELIX 542..559 FT /evidence="ECO:0007829|PDB:6YG9" FT STRAND 561..563 FT /evidence="ECO:0007829|PDB:1E7A" FT HELIX 565..583 FT /evidence="ECO:0007829|PDB:1N5U" FT STRAND 584..587 FT /evidence="ECO:0007829|PDB:1N5U" FT HELIX 588..590 FT /evidence="ECO:0007829|PDB:2BXG" FT TURN 591..593 FT /evidence="ECO:0007829|PDB:1N5U" FT HELIX 596..602 FT /evidence="ECO:0007829|PDB:6YG9" FT TURN 603..605 FT /evidence="ECO:0007829|PDB:6YG9" SQ SEQUENCE 609 AA; 69367 MW; F88FF61DD242E818 CRC64; MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV AASQAALGL //